Dimerization of recombinant horseradish peroxidase in a reversed micellar system.
Recombinant horseradish peroxidase reactivated from E. coli inclusion bodies was studied in a reversed micellar system of AOT in octane. The ability of the recombinant enzyme, in contrast to native horseradish peroxidase, to form a dimeric structure was found. The existence of the dimer was proved by results of sedimentation analysis. Dimer/monomer ratio in the enzyme-containing micelles and dimer catalytic activity were found to depend on the substrate used (pyrogallol, guaiacol, o-dianisidine, o-phenylenediamine). Computer modelling was used to describe possible structures of the dimeric recombinant horseradish peroxidase.
Klyachko
N L
NL
School of Chemistry, Lomonosov Moscow State University, Moscow, Russia.
Dulkis YuK
Gazaryan
I G
IG
Ouporov
I V
IV
Levashov
A V
AV
D019281:Dimerization; D004143:Dioctyl Sulfosuccinic Acid / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006861:Hydrogen Peroxide; D007700:Kinetics; D008823:Micelles; D008958:Models, Molecular; D009795:Octanes / Q000378:metabolism; D010636:Phenols / Q000378:metabolism; D010655:Phenylenediamines / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D014461:Ultracentrifugation
D008823:Micelles; D009795:Octanes; D010636:Phenols; D010655:Phenylenediamines; D011994:Recombinant Proteins; D004143:Dioctyl Sulfosuccinic Acid; D006861:Hydrogen Peroxide; D006735:Horseradish Peroxidase; C026728:octane